Results 11 to 20 of about 62,512 (285)

Single-Molecule FRET of Membrane Transport Proteins. [PDF]

open access: yesChembiochem, 2021
AbstractUncovering the structure and function of biomolecules is a fundamental goal in structural biology. Membrane‐embedded transport proteins are ubiquitous in all kingdoms of life. Despite structural flexibility, their mechanisms are typically studied by ensemble biochemical methods or by static high‐resolution structures, which complicate a ...
Bartels K   +3 more
europepmc   +5 more sources

High-Resolution Single-Molecule FRET via DNA eXchange (FRET X) [PDF]

open access: yesNano Letters, 2020
ABSTRACTSingle-molecule FRET is a versatile tool to study nucleic acids and proteins at the nanometer scale. However, currently, only a couple of FRET pairs can be reliably measured on a single object. The limited number of available FRET pair fluorophores and complicated data analysis makes it challenging to apply single-molecule FRET for structural ...
Mike Filius   +3 more
openaire   +5 more sources

Unmasking a two-faced protein

open access: yeseLife, 2022
Single-molecule fluorescence spectroscopy and molecular dynamics simulations illuminate the structure and dynamics of PSD-95, a protein involved in neural plasticity.
Ivan Maslov, Jelle Hendrix
doaj   +1 more source

On the statistical foundation of a recent single molecule FRET benchmark [PDF]

open access: yesNature Communications
Ayush Saurabh   +2 more
doaj   +2 more sources

Signal Transduction Mechanisms Quantitatively Observed One Molecule at a Time

open access: yesFrontiers in Physics, 2022
Improved single-molecule methods can largely increase our understanding of underlying molecular mechanism during cellular signal transduction. In contrast to conventional bulk methods, monitoring molecules one at a time can circumvent averaging effects ...
Pei Li   +4 more
doaj   +1 more source

Single-Molecule Three-Color FRET [PDF]

open access: yesBiophysical Journal, 2004
Fluorescence resonance energy transfer (FRET) measured at the single-molecule level can reveal conformational changes of biomolecules and intermolecular interactions in physiologically relevant conditions. Thus far single-molecule FRET has been measured only between two fluorophores.
Hohng, Sungchul   +2 more
openaire   +2 more sources

Single‐Molecule Four‐Color FRET [PDF]

open access: yesAngewandte Chemie International Edition, 2010
We developed a single-molecule four-color FRET technique both in confocal and in total-internal-reflection fluorescence microscopies. Real-time determination of six inter-fluorophore FRET efficiencies allowed us to probe the correlated motion of four arms of the Holliday junction.
Jinwoo, Lee   +5 more
openaire   +2 more sources

Single-Molecule FRET Detection of Sub-Nanometer Distance Changes in the Range below a 3-Nanometer Scale

open access: yesBiosensors, 2020
Single-molecule fluorescence energy transfer (FRET) detection has become a key technique to monitor intra- and intermolecular distance changes in biological processes.
Heyjin Son   +4 more
doaj   +1 more source

Single-Molecule FRET Analyses of NMDA Receptors. [PDF]

open access: yesMethods Mol Biol
Single-molecule fluorescence resonance energy transfer (smFRET) enables the real-time observation of conformational changes in a single protein molecule of interest. These observations are achieved by attaching fluorophores to proteins of interest in a site-specific manner and investigating the FRET between the fluorophores. Here we describe the method
Durham RJ, Jayaraman V.
europepmc   +3 more sources

Single-Molecule FRET-Based Dynamic DNA Sensor. [PDF]

open access: yesACS Sens, 2021
Selective and sensitive detection of nucleic acid biomarkers is of great significance in early-stage diagnosis and targeted therapy. Therefore, the development of diagnostic methods capable of detecting diseases at the molecular level in biological fluids is vital to the emerging revolution in the early diagnosis of diseases. However, the vast majority
Megalathan A, Wijesinghe KM, Dhakal S.
europepmc   +3 more sources

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